3POS
Crystal structure of the globular domain of human calreticulin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006457 | biological_process | protein folding |
| A | 0051082 | molecular_function | unfolded protein binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006457 | biological_process | protein folding |
| B | 0051082 | molecular_function | unfolded protein binding |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0006457 | biological_process | protein folding |
| C | 0051082 | molecular_function | unfolded protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1 |
| Chain | Residue |
| A | GLN26 |
| A | LYS62 |
| A | LYS64 |
| A | ASP328 |
| A | HOH728 |
| A | HOH730 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2 |
| Chain | Residue |
| B | ASP328 |
| B | HOH725 |
| B | HOH726 |
| B | GLN26 |
| B | LYS62 |
| B | LYS64 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 3 |
| Chain | Residue |
| C | GLN26 |
| C | LYS62 |
| C | LYS64 |
| C | ASP328 |
| C | HOH727 |
| C | HOH729 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"1-1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 358 |
| Details | Region: {"description":"N-domain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21423620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27840680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3POS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3POW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14211","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
